ID   NAPA_HAEI8              Reviewed;         827 AA.
AC   Q4QNJ6;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=NTHI0463;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable
RT   Haemophilus influenzae: comparative study with H. influenzae serotype
RT   d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
CC   -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC       (NAP). Only expressed at high levels during aerobic growth. NapAB
CC       complex receives electrons from the membrane-anchored tetraheme
CC       protein napC, thus allowing electron flow between membrane and
CC       periplasm. Essential function for nitrate assimilation and may
CC       have a role in anaerobic metabolism (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
CC       acceptor.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
CC   -!- COFACTOR: Binds 1 molybdenum ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups
CC       per subunit (By similarity).
CC   -!- SUBUNIT: Interacts with napB (By similarity).
CC   -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/napA/narB subfamily.
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DR   EMBL; CP000057; AAX87401.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_248061.1; -.
DR   SMR; Q4QNJ6; 37-825.
DR   GeneID; 3429783; -.
DR   GenomeReviews; CP000057_GR; NTHI0463.
DR   KEGG; hit:NTHI0463; -.
DR   HOGENOM; Q4QNJ6; -.
DR   BioCyc; HINF281310:NTHI0463-MON; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:HAMAP.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:HAMAP.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:HAMAP.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_01630; -; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_fold.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_Fe4S4.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR006657; MPT_dinuc_bd.
DR   InterPro; IPR010051; NO3_reductase_lsu_periplasm.
DR   InterPro; IPR006311; Tat.
DR   InterPro; IPR019546; TAT_signal.
DR   InterPro; IPR017909; Twin_arg_translocation_Tat.
DR   Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF10518; TAT_signal; 1.
DR   TIGRFAMs; TIGR01706; NAPA; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; FALSE_NEG.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase;
KW   Periplasm; Signal; Transport.
FT   SIGNAL        1     33       Tat-type signal (Potential).
FT   CHAIN        34    827       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000045988.
FT   METAL        44     44       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        47     47       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        51     51       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        79     79       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   827 AA;  93629 MW;  4D798077DCB23060 CRC64;
     MNLSRRDFMK ANAAMAAATA AGLTIPVKNV VAAESEIKWD KAVCRFCGTG CAVLVGTKDG
     RVVASQGDPD AEVNRGLNCI KGYFLPKIMY GKDRLTQPLL RMTNGKFDKN GDFAPVSWDF
     AFKTMAEKFK EAFKKNGQNA VGMFSSGQST IWEGYAKNKL WKAGFRSNNV DPNARHCMAS
     AAVAFMRTFG MDEPMGCYDD IEQADAFVLW GSNMAEMHPI LWSRITDRRI SNPDVRVTVL
     STYEHRSFEL ADHGLIFTPQ TDLAIMNYII NYLIQNNAIN WDFVNKHTKF KRGETNIGYG
     LRPEHPLEKD TNRATAGKMH DSSFEELKQL VSEYTVEKVS KMSGLDKVQL ETLAKLYADP
     TKKVVSYWTM GFNQHTRGVW VNQLIYNIHL LTGKISIPGC GPFSLTGQPS ACGTAREVGS
     FPHRLPADLV VTNPKHRETA ERIWKLPKGT VSEKVGLHTI AQDRAMNDGE MNVLWQMCNN
     NMQAGPNINQ ERLPGWRKEG NFVIVSDPYP TVSALSADLI LPTAMWVEKE GAYGNAERRT
     QFWRQQVKAP GEAKSDLWQL MEFAKYFTTD EMWTEDLLTQ MPEYRGKTLY EVLFKNGQVD
     KFPLSELAEG QLNDESEYFG YYVHKGLFEE YAEFGRGHGH DLAPFDMYHK AHGLRWPVVE
     GKETLWRYRE GYDPYVKEGE GVAFYGYPDK KAIILAVPYE PPAESPDNEY DLWLSTGRVL
     EHWHTGTMTR RVPELHRAFP NNLVWMHPLD AQARGLRHGD KIKISSRRGE MISYLDTRGR
     NKPPRGLVFT TFFDAGQLAN SLTLDATDPI SKETDFKKCA VKVEKAA
//